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Reviewed, UniProtKB/Swiss-Prot P31210 (AK1D1_RAT)

Last modified June 16, 2009. Version 72. 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-oxo-5-beta-steroid 4-dehydrogenase
    EC=1.3.1.3
Alternative name(s):
    Delta(4)-3-ketosteroid 5-beta-reductase
    Delta(4)-3-oxosteroid 5-beta-reductase
    Aldo-keto reductase family 1 member D1
Gene names
Name: Akr1d1
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length326 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Efficiently catalyzes the reduction of progesterone, androstenedione, 17-alpha-hydroxyprogesterone and testosterone to 5-beta-reduced metabolites. The bile acid intermediates 7-alpha,12-alpha-dihydroxy-4-cholesten-3-one and 7-alpha-hydroxy-4-cholesten-3-one can also act as substrates.

Catalytic activity

5-beta-cholestan-3-one + NADP+ = cholest-4-en-3-one + NADPH.

17,21-dihydroxy-5-beta-pregnane-3,11,20-trione + NADP+ = cortisone.

Subcellular location

Cytoplasm.

Post-translational modification

The N-terminus is blocked.

Sequence similarities

Belongs to the aldo/keto reductase family.

Ontologies

Keywords
   Biological processBile acid catabolism
Lipid metabolism
Steroid metabolism
   Cellular componentCytoplasm
   LigandNADP
   Molecular functionOxidoreductase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processbile acid catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function3-oxo-5-beta-steroid 4-dehydrogenase activity Ref.2

Inferred from direct assay. Source: MGI

delta4-3-oxosteroid 5beta-reductase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3263263-oxo-5-beta-steroid 4-dehydrogenase
PRO_0000124672

Regions

Nucleotide binding168 – 1692NADP By similarity
Nucleotide binding220 – 2245NADP By similarity
Nucleotide binding273 – 28311NADP By similarity

Sites

Active site571Proton donor By similarity
Binding site521NADP By similarity
Binding site1921NADP By similarity
Binding site2301Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P31210-1 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 32D8266BFA62CE99

FASTA32637,378
        10         20         30         40         50         60 
MNLSTANHHI PLNDGNSIPI IGLGTYSDPR PVPGKTFIAV KTAIDEGYRH IDGAYVYRNE 

        70         80         90        100        110        120 
HEVGEAIREK VAEGKVKREE IFYCGKLWST DHDPEMVRPA LERTLQTLKL DYIDLYIIEM 

       130        140        150        160        170        180 
PMAFKPGEEF YPKDENGRVI YHKSNLCATW EALEACKDAG LVKSLGVSNF NRRQLEVILN 

       190        200        210        220        230        240 
KPGLKYKPVT NQVECHPYFT QTKLLEVSAS SMTSFIVAYS PLGTCRNPLW VNVSSPPLLK 

       250        260        270        280        290        300 
DELLTSLGKK YNKTQAQIVL RFDIQRGLVV IPKSTTPERI KENFQIFDFS LTKEEMKDIE 

       310        320 
ALNKNVRFVE MLMWSDHPEY PFHDEY 

« Hide

References

[1]"Molecular cloning and sequence analysis of cDNA encoding delta 4-3-ketosteroid 5 beta-reductase of rat liver."
Onishi Y., Noshiro M., Shimosato T., Okuda K.
FEBS Lett. 283:215-218(1991) [PubMed: 1710579] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"Delta 4-3-Oxosteroid 5 beta-reductase. Structure and function."
Onishi Y., Noshiro M., Shimosato T., Okuda K.
Biol. Chem. Hoppe-Seyler 372:1039-1049(1991) [PubMed: 1789929] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Liver.
[3]"Identification of the 37-kd rat liver protein that forms an acetaldehyde adduct in vivo as delta 4-3-ketosteroid 5 beta-reductase."
Zhu Y., Fillenwarth M.J., Crabb D., Lumeng L., Lin R.C.
Hepatology 23:115-122(1996) [PubMed: 8550030] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.

Cross-references

Sequence databases

D17309 mRNA. Translation: BAA04131.1.
S80431 mRNA. Translation: AAB35916.2.
IPIIPI00210823.
PIRS15835.
RefSeqNP_620239.1.
UniGeneRn.25716

3D structure databases

HSSPHSSP built from PDB template 1LWI based on UniProtKB P23457.
ModBaseSearch...

Proteomic databases

PRIDEP31210.

Genome annotation databases

EnsemblENSRNOG00000013004. Rattus norvegicus. [Contig view]
GeneID192242.
KEGGrno:192242.

Organism-specific databases

RGD620752. Akr1d1.

Phylogenomic databases

HOVERGENP31210.

Enzyme and pathway databases

BRENDA1.3.1.3. 248.

Gene expression databases

ArrayExpressP31210.
GermOnlineENSRNOG00000013004. Rattus norvegicus.

Family and domain databases

InterProIPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
[Graphical view]
Gene3DG3DSA:3.20.20.100. Aldo/ket_red. 1 hit.
PANTHERPTHR11732. Aldo/ket_red. 1 hit.
PfamPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
ProDomPD000288. Aldo/ket_red. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio622866.

Entry information

Entry nameAK1D1_RAT
AccessionPrimary (citable) accession number: P31210
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: June 16, 2009
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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