Reviewed,
UniProtKB/Swiss-Prot Q5RBB9 (NQO2_PONAB)
Last modified
February 9, 2010.
Version 32.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Ribosyldihydronicotinamide dehydrogenase [quinone] EC=1.10.99.2 Alternative name(s): NRH dehydrogenase [quinone] 2 NRH:quinone oxidoreductase 2 Quinone reductase 2 Short name=QR2 | ||
| 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 | 231 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinones involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis By similarity. |
| Catalytic activity | 1-(beta-D-ribofuranosyl)-1,4-dihydronicotinamide + a quinone = 1-(beta-D-ribofuranosyl)nicotinamide + a hydroquinone. |
| Cofactor | Binds 1 zinc ion per subunit By similarity. FAD By similarity. |
| Subunit structure | Homodimer By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Miscellaneous | Uses dihydronicotinamide riboside (NRH) rather than NAD(P)H as an electron donor. |
| Sequence similarities | Belongs to the NAD(P)H dehydrogenase (quinone) family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | FAD Flavoprotein Metal-binding Zinc |
| Molecular function | Oxidoreductase |
| PTM | Phosphoprotein |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | coenzyme binding Inferred from electronic annotation. Source: InterPro dihydronicotinamide riboside quinone reductase activityInferred from electronic annotation. Source: EC electron carrier activityInferred from electronic annotation. Source: InterPro 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 231 | 230 | Ribosyldihydronicotinamide dehydrogenase [quinone] | PRO_0000071628 | |||||
Regions | |||||||||
| Nucleotide binding | 18 – 21 | 4 | FAD By similarity | ||||||
| Nucleotide binding | 104 – 107 | 4 | FAD By similarity | ||||||
| Nucleotide binding | 148 – 151 | 4 | FAD By similarity | ||||||
| Region | 127 – 129 | 3 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Metal binding | 174 | 1 | Zinc By similarity | ||||||
| Metal binding | 178 | 1 | Zinc By similarity | ||||||
| Metal binding | 223 | 1 | Zinc By similarity | ||||||
| Binding site | 12 | 1 | FAD By similarity | ||||||
| Binding site | 156 | 1 | FAD By similarity | ||||||
| Binding site | 194 | 1 | FAD By similarity | ||||||
| Binding site | 201 | 1 | FAD By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 31 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 80 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 197 | 1 | Phosphoserine 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: Kidney. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CR858732 mRNA. Translation: CAH90941.1. |
| RefSeq | NP_001127353.1. |
| UniGene | Pab.13785 |
3D structure databases | |
| SMR | Q5RBB9. Positions 2-231. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 100174417. |
Organism-specific databases | |
| CTD | 100174417. |
Phylogenomic databases | |
| HOVERGEN | Q5RBB9. |
| InParanoid | Q5RBB9. |
Enzyme and pathway databases | |
| BRENDA | 1.10.99.2. 269192. |
Family and domain databases | |
| InterPro | IPR003680. Flavodoxin_fold. [Graphical view] |
| Pfam | PF02525. Flavodoxin_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | NQO2_PONAB | ||||||||
| Accession | Primary (citable) accession number: Q5RBB9 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

Clusters with


