Reviewed,
UniProtKB/Swiss-Prot P80702 (DIDH_COMTE)
Last modified
June 16, 2009.
Version 38.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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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 HSD28 |
| Organism | Comamonas testosteroni (Pseudomonas testosteroni) |
| Taxonomic identifier | 285 [NCBI] |
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Comamonadaceae › Comamonas |
Protein attributes
| Sequence length | 30 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 | |
| Induction | By steroids. |
| 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-SubCell |
| Molecular function | 3-alpha-hydroxysteroid dehydrogenase (B-specific) activity Inferred 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 – ›30 | ›30 | 3-alpha-hydroxysteroid dehydrogenase | PRO_0000054656 | |||||
Regions | |||||||||
| Region | 10 – ›30 | ›21 | Involved in cofactor binding By similarity | ||||||
Sites | |||||||||
| Binding site | 29 | 1 | Substrate By similarity | ||||||
Experimental info | |||||||||
| Non-terminal residue | 30 | 1 | |||||||
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. Strain: ATCC 11996 / DSM 50244 / JCM 5832 / NCIB 8955 / NCTC 10698. |
Cross-references
3D structure databases | |
|---|---|
| HSSP | HSSP built from PDB template 1FK8 based on UniProtKB Q9ZFY9. |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 1.1.1.50. 4566. |
Family and domain databases | |
| InterPro | IPR002198. DH_sc/Rdtase_SDR. [Graphical view] |
| PROSITE | PS00061. ADH_SHORT. Partial match. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DIDH_COMTE | ||||||||
| Accession | Primary (citable) accession number: P80702 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

Clusters with


