Reviewed,
UniProtKB/Swiss-Prot Q9TV70 (DHDH_RABIT)
Last modified
June 16, 2009.
Version 36.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase EC=1.3.1.20 Alternative name(s): Dimeric dihydrodiol dehydrogenase D-xylose-NADP dehydrogenase EC=1.1.1.179 D-xylose 1-dehydrogenase ORY2DD | ||||
| Gene names |
| ||||
| Organism | Oryctolagus cuniculus (Rabbit) | ||||
| Taxonomic identifier | 9986 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus |
Protein attributes
| Sequence length | 329 AA. |
| Sequence status | Fragment. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Catalytic activity | Trans-1,2-dihydrobenzene-1,2-diol + NADP+ = catechol + NADPH. D-xylose + NADP+ = D-xylono-1,5-lactone + NADPH. |
| Enzyme regulation | Stimulated by various salts. Ref.2 |
| Subunit structure | Homodimer. Ref.1 |
| Tissue specificity | Lens, liver and small intestine. Ref.1 |
| Sequence similarities | Belongs to the gfo/idh/mocA family. |
| biophysicochemical properties | Kinetic parameters: KM=4.4 mM for D-xylose Vmax=3.6 µmol/min/mg enzyme with D-xylose as substrate |
Ontologies
| Keywords | |
|---|---|
| Ligand | NADP |
| Molecular function | Oxidoreductase |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | D-xylose 1-dehydrogenase (NADP+) activity Inferred from electronic annotation. Source: EC bindingInferred from electronic annotation. Source: InterPro electron carrier activityInferred from electronic annotation. Source: InterPro trans-1,2-dihydrobenzene-1,2-diol dehydrogenase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | ‹1 – 329 | ›329 | Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase | PRO_0000315367 | |||||
Sites | |||||||||
| Site | 65 | 1 | May play an important role in coenzyme binding By similarity | ||||||
| Site | 73 | 1 | May play an important role in coenzyme binding By similarity | ||||||
| Site | 91 | 1 | May play an important role in coenzyme binding By similarity | ||||||
| Site | 170 | 1 | May play an important role for the adaptation of the alcohol substrate into the binding site By similarity | ||||||
| Site | 174 | 1 | May play an important role in catalytic activity By similarity | ||||||
Experimental info | |||||||||
| Non-terminal residue | 1 | 1 | |||||||
Sequences
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References
| [1] | "Cloning and sequencing of the cDNA species for mammalian dimeric dihydrodiol dehydrogenases." Arimitsu E., Aoki S., Ishikura S., Nakanishi K., Matsuura K., Hara A. Biochem. J. 342:721-728(1999) [PubMed: 10477285] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, TISSUE SPECIFICITY. Tissue: Lens. |
| [2] | "Identity of dimeric dihydrodiol dehydrogenase as NADP(+)-dependent D-xylose dehydrogenase in pig liver." Aoki S., Ishikura S., Asada Y., Usami N., Hara A. Chem. Biol. Interact. 130:775-784(2001) [PubMed: 11306093] [Abstract] Cited for: ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. Tissue: Lens. |
Cross-references
Sequence databases | |
|---|---|
| AB021928 mRNA. Translation: BAA83485.1. | |
| UniGene | Ocu.6266 |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| Ensembl | ENSOCUG00000006419. Oryctolagus cuniculus. [Contig view] |
Phylogenomic databases | |
| HOVERGEN | Q9TV70. |
Enzyme and pathway databases | |
| BRENDA | 1.1.1.179. 255. 1.3.1.20. 255. |
Family and domain databases | |
| InterPro | IPR016040. NAD(P)-bd_dom. IPR000683. Oxidoreductase_N. IPR004104. OxRdtase_C. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| Pfam | PF01408. GFO_IDH_MocA. 1 hit. PF02894. GFO_IDH_MocA_C. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DHDH_RABIT | ||||||||
| Accession | Primary (citable) accession number: Q9TV70 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

Clusters with


