Reviewed,
UniProtKB/Swiss-Prot Q9TV68 (DHDH_CANFA)
Last modified
February 9, 2010.
Version 46.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
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 Can2DD | ||||
| Gene names |
| ||||
| Organism | Canis familiaris (Dog) | ||||
| Taxonomic identifier | 9615 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis |
Protein attributes
| Sequence length | 335 AA. |
| Sequence status | Complete. |
| 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 | Strongly inhibited by isoascorbic acid, 4-hydroxyacetophenone and 4-chloromercuriphenylsulphonate. Stimulated by various salts. Ref.2 Ref.3 |
| Subunit structure | Homodimer. Ref.1 |
| Tissue specificity | Liver and kidney. Ref.1 |
| Sequence similarities | Belongs to the gfo/idh/mocA family. |
| Biophysicochemical properties | Kinetic parameters: KM=1.6 mM for naphthalene dihydrodiol (at pH 7.5) KM=0.27 mM for benzene dihydrodiol (at pH 7.5) KM=1.6 mM for D-xylose KM=0.68 mM for 3-deoxyglucosone (at pH 7.5) KM=0.07 mM for camphorquinone (at pH 7.5) KM=0.59 mM for methylglyoxal (at pH 7.5) Vmax=3.27 µmol/min/mg enzyme with naphthalene dihydrodiol as substrate (at pH 7.5) Vmax=2.76 µmol/min/mg enzyme with benzene dihydrodiol as substrate (at pH 7.5) Vmax=4.4 µmol/min/mg enzyme with D-xylose as substrate Vmax=3.55 µmol/min/mg enzyme with reduced 3-deoxyglucosone as substrate (at pH 7.5) Vmax=5.54 µmol/min/mg enzyme with camphorquinone as substrate (at pH 7.5) Vmax=3.11 µmol/min/mg enzyme with methylglyoxal as substrate (at pH 7.5) |
Ontologies
| Keywords | |
|---|---|
| Ligand | NADP |
| Molecular function | Oxidoreductase |
| Technical term | Direct protein sequencing |
| 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 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 – 335 | 335 | Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase | PRO_0000315360 | |||||
Sites | |||||||||
| Site | 71 | 1 | May play an important role in coenzyme binding By similarity | ||||||
| Site | 79 | 1 | May play an important role in coenzyme binding By similarity | ||||||
| Site | 97 | 1 | May play an important role in coenzyme binding By similarity | ||||||
| Site | 176 | 1 | May play an important role for the adaptation of the alcohol substrate into the binding site By similarity | ||||||
| Site | 180 | 1 | May play an important role in catalytic activity By similarity | ||||||
Sequences
| ||||||||||||||||||
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], PROTEIN SEQUENCE OF 54-80; 92-114; 157-191; 245-262; 277-291; 303-323 AND 325-333, SUBUNIT, TISSUE SPECIFICITY. Tissue: Liver. |
| [2] | "Purification and characterization of dimeric dihydrodiol dehydrogenase from dog liver." Sato K., Nakanishi M., Deyashiki Y., Hara A., Matsuura K., Ohya I. J. Biochem. 116:711-717(1994) [PubMed: 7852295] [Abstract] Cited for: ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. |
| [3] | "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: Liver. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AB021930 mRNA. Translation: BAA83487.1. |
| RefSeq | NP_001003160.1. |
| UniGene | Cfa.3648 |
3D structure databases | |
| SMR | Q9TV68. Positions 2-333. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q9TV68. |
Genome annotation databases | |
| Ensembl | ENSCAFT00000006229; ENSCAFP00000005770; ENSCAFG00000003869; Canis familiaris. [Genome view] |
| GeneID | 403786. |
| KEGG | cfa:403786. |
Organism-specific databases | |
| CTD | 403786. |
Phylogenomic databases | |
| eggNOG | maNOG16421. |
| HOVERGEN | Q9TV68. |
| InParanoid | Q9TV68. |
| OMA | DSHAQYA. |
| OrthoDB | EOG9NZXD5. |
| PhylomeDB | Q9TV68. |
Enzyme and pathway databases | |
| BRENDA | 1.1.1.179. 463. 1.3.1.20. 463. |
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_CANFA | ||||||||
| Accession | Primary (citable) accession number: Q9TV68 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

Clusters with


