Q5RCY2 (NUDT5_PONAB) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 44.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: ADP-sugar pyrophosphatase EC=3.6.1.- EC=3.6.1.13 Alternative name(s): Nucleoside diphosphate-linked moiety X motif 5 Short name=Nudix motif 5 | ||
| Gene names |
| ||
| Organism | Pongo abelii (Sumatran orangutan) | ||
| Taxonomic identifier | 9601 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo |
Protein attributes
| Sequence length | 216 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | Hydrolyzes with similar activities ADP-ribose, ADP-mannose, and ADP-glucose. Can also hydrolyze other nucleotide sugars with low activity By similarity. |
| Catalytic activity | ADP-ribose + H2O = AMP + D-ribose 5-phosphate. ADP-sugar + H2O = AMP + alpha-D-aldose 1-phosphate. |
| Cofactor | Binds 3 magnesium ions per subunit By similarity. |
| Subunit structure | Homodimer By similarity. |
| Sequence similarities | Belongs to the Nudix hydrolase family. Contains 1 nudix hydrolase domain. |
Ontologies
| Keywords | |
|---|---|
| Ligand | Magnesium Metal-binding |
| Molecular function | Hydrolase |
| PTM | Acetylation Phosphoprotein |
| Gene Ontology (GO) | |
| Biological process | ribonucleoside diphosphate catabolic process Inferred from sequence or structural similarity. Source: UniProtKB |
| Molecular function | ADP-ribose diphosphatase activity Inferred from electronic annotation. Source: EC magnesium ion bindingInferred from sequence or structural similarity. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 216 | 216 | ADP-sugar pyrophosphatase | PRO_0000250702 | |||||
Regions | |||||||||
| Domain | 57 – 194 | 138 | Nudix hydrolase | ||||||
| Region | 46 – 47 | 2 | Substrate binding; shared with dimeric partner By similarity | ||||||
| Motif | 97 – 118 | 22 | Nudix box | ||||||
Sites | |||||||||
| Metal binding | 96 | 1 | Magnesium 1; via carbonyl oxygen By similarity | ||||||
| Metal binding | 112 | 1 | Magnesium 2 By similarity | ||||||
| Metal binding | 112 | 1 | Magnesium 3 By similarity | ||||||
| Metal binding | 116 | 1 | Magnesium 1 By similarity | ||||||
| Metal binding | 116 | 1 | Magnesium 3 By similarity | ||||||
| Metal binding | 163 | 1 | Magnesium 3 By similarity | ||||||
| Binding site | 28 | 1 | Substrate By similarity | ||||||
| Binding site | 51 | 1 | Substrate; shared with dimeric partner By similarity | ||||||
| Binding site | 84 | 1 | Substrate By similarity | ||||||
| Binding site | 98 | 1 | Substrate; via amide nitrogen By similarity | ||||||
| Binding site | 133 | 1 | Substrate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 1 | 1 | N-acetylmethionine By similarity | ||||||
| Modified residue | 9 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 10 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 42 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 74 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 207 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 215 | 1 | N6-acetyllysine By similarity | ||||||
Sequences
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References
| [1] | The German cDNA consortium Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Heart. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CR858136 mRNA. Translation: CAH90375.1. |
| RefSeq | NP_001125182.1. NM_001131710.1. |
| UniGene | Pab.13961. |
3D structure databases | |
| ProteinModelPortal | Q5RCY2. |
| SMR | Q5RCY2. Positions 14-216. |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | Q5RCY2. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSPPYT00000002500; ENSPPYP00000002426; ENSPPYG00000002091. |
| GeneID | 100172071. |
| KEGG | pon:100172071. |
Organism-specific databases | |
| CTD | 11164. |
Phylogenomic databases | |
| HOVERGEN | HBG052691. |
Family and domain databases | |
| InterPro | IPR020476. Nudix_hydrolase. IPR020084. NUDIX_hydrolase_CS. IPR000086. NUDIX_hydrolase_dom. IPR015797. NUDIX_hydrolase_dom-like. [Graphical view] |
| Gene3D | G3DSA:3.90.79.10. NUDIX_hydrolase. 1 hit. |
| KO | K13987. |
| Pfam | PF00293. NUDIX. 1 hit. [Graphical view] |
| PRINTS | PR00502. NUDIXFAMILY. |
| SUPFAM | SSF55811. NUDIX_hydrolase. 1 hit. |
| PROSITE | PS51462. NUDIX. 1 hit. PS00893. NUDIX_BOX. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | NUDT5_PONAB | ||||||||
| Accession | Primary (citable) accession number: Q5RCY2 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with