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Reviewed, UniProtKB/Swiss-Prot P80701 (DIDH_PSESP)

Last modified November 4, 2008. Version 30. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    3-alpha-hydroxysteroid dehydrogenase
      Short name=3-alpha-HSD
    EC=1.1.1.50
Alternative name(s):
    Hydroxyprostaglandin dehydrogenase
    HSD29
OrganismPseudomonas sp.
Taxonomic identifier306 [NCBI]
Taxonomic lineageBacteriaProteobacteria

Protein attributes

Sequence length15 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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

Cytoplasm.

Sequence similarities

Belongs to the short-chain dehydrogenases/reductases (SDR) family.

Ontologies

Keywords

   Cellular componentCytoplasm
   LigandNAD
   Molecular functionOxidoreductase
   Technical termDirect protein sequencing

Gene Ontology (GO)

   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular function3-alpha-hydroxysteroid dehydrogenase (B-specific) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›15›153-alpha-hydroxysteroid dehydrogenase
PRO_0000054657

Regions

Region6 – ›15›10Involved in cofactor binding By similarity

Experimental info

Non-terminal residue151

Sequences

Sequence LengthMass (Da)Tools
P80701-1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 9506860D070A7790

FASTA151,315
        10 
QVIAITGSAS GIGAA 

« Hide

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

ModBaseSearch...

Family and domain databases

InterProIPR002198. DHase_sc/Rdtase_SDR.
[Graphical view]
PROSITEPS00061. ADH_SHORT. Partial match.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDIDH_PSESP
AccessionPrimary (citable) accession number: P80701
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 4, 2008
This is version 30 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents