Reviewed,
UniProtKB/Swiss-Prot P80701 (DIDH_PSESP)
Last modified
November 4, 2008.
Version 30.
History...
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: 3-alpha-hydroxysteroid dehydrogenase Short name=3-alpha-HSD EC=1.1.1.50 Alternative name(s): Hydroxyprostaglandin dehydrogenase HSD29 |
| Organism | Pseudomonas sp. |
| Taxonomic identifier | 306 [NCBI] |
| Taxonomic lineage | Bacteria › Proteobacteria |
Protein attributes
| Sequence length | 15 AA. |
| Sequence status | Fragment. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Along with the 3 alpha-hydroxysteroid dehydrogenase and 3-oxo-reductase activities towards a variety of cis or trans fused A/B ring steroids, it also reduces several xenobiotic carbonyl compounds, including a metyrapone-based class of insecticides, to the respective alcohol metabolites. |
| Catalytic activity | Androsterone + NAD(P)(+) = 5-alpha-androstane-3,17-dione + NAD(P)H. |
| Subcellular location | |
| Sequence similarities | Belongs to the short-chain dehydrogenases/reductases (SDR) family. |
Ontologies
Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| Technical term | Direct protein sequencing |
Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | 3-alpha-hydroxysteroid dehydrogenase (B-specific) activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
References
| [1] | "Characterization of a 3 alpha-hydroxysteroid dehydrogenase/carbonyl reductase from the Gram-negative bacterium Comamonas testosteroni." Oppermann U.C.T., Maser E. Eur. J. Biochem. 241:744-749(1996) [PubMed: 8944761] [Abstract] Cited for: PROTEIN SEQUENCE. |
Cross-references
3D structure databases | |
|---|---|
| ModBase | Search... |
Family and domain databases | |
| InterPro | IPR002198. DHase_sc/Rdtase_SDR. [Graphical view] |
| PROSITE | PS00061. ADH_SHORT. Partial match. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DIDH_PSESP | ||||||||
| Accession | Primary (citable) accession number: P80701 | ||||||||
| 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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